Teruo Ogawa
Research Subjects
Teruo Ogawa has a total of 29 co-authors. Here are the top co-authors by number of shared publications:
- Aaron Kaplan
Department of Plants and Environmental Science, The Hebrew University of Jerusalem, Edmond Safra Campus, Jerusalem 9190400, Israel
3 shared publications - Fudan Gao
Shanghai Engineering Research Center of Plant Germplasm Resources, Shanghai Collaborative Innovation Center of Plant Germplasm Resources Development, College of Life Sciences, Shanghai Normal University , Shanghai 200234
3 shared publications Jiaohong Zhao
College of Life and Environment Sciences, Shanghai Normal University, Shanghai 200234, China (F.G., J.Z., L.C., Z.R., W.M.).
3 shared publications- Weimin Ma
College of Life Sciences Shanghai Normal University Shanghai China
3 shared publications Hualing Mi
National Laboratory of Plant Molecular Genetics, Institute of Plant Physiology and Ecology, Shanghai Institute for Biological Sciences, Graduate courses of the Chinese Academy of Sciences, Shanghai, 200032, PR China
2 shared publicationsAaron Kaplan
The Hebrew University of Jerusalem
1 shared publication
Latest Publications
- 13 February 2021
- Published by Springer Nature in Photosynthesis Research
- Vol. 147 (3) , 243-252
Honoring Bacon Ke at 100: a legend among the many luminaries and a highly collaborative scientist in photosynthesis research
Bacon Ke, who did pioneering research on the primary photochemistry of photosynthesis, was born in China on July 26, 1920, and currently, he is living in a senior home in San Francisco, California, and is a centenarian. To us, this is a very happy and unique occasion to honor him. After providing a brief account of his life, and a glimpse of his research in photosynthesis, we present here “messages” for Bacon Ke@ 100 from: Robert Alfano (USA), Charles Arntzen (USA), Sandor Demeter (Hungary), Richard A. Dilley (USA), John Golbeck (USA), Isamu Ikegami (Japan), Ting-Yun Kuang (China), Richard Malkin (USA), Hualing Mi (China), Teruo Ogawa (Japan), Yasusi Yamamoto (Japan), and Xin-Guang Zhu (China).
- 13 February 2021
- Published by Springer Nature in Photosynthesis Research
- Vol. 147 (3) , 243-252
Honoring Bacon Ke at 100: a legend among the many luminaries and a highly collaborative scientist in photosynthesis research
Bacon Ke, who did pioneering research on the primary photochemistry of photosynthesis, was born in China on July 26, 1920, and currently, he is living in a senior home in San Francisco, California, and is a centenarian. To us, this is a very happy and unique occasion to honor him. After providing a brief account of his life, and a glimpse of his research in photosynthesis, we present here “messages” for Bacon Ke@ 100 from: Robert Alfano (USA), Charles Arntzen (USA), Sandor Demeter (Hungary), Richard A. Dilley (USA), John Golbeck (USA), Isamu Ikegami (Japan), Ting-Yun Kuang (China), Richard Malkin (USA), Hualing Mi (China), Teruo Ogawa (Japan), Yasusi Yamamoto (Japan), and Xin-Guang Zhu (China).
- Open Access
- 12 September 2016
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 172 (3) , 1451-1464
The NDH-1L-PSI Supercomplex Is Important for Efficient Cyclic Electron Transport in Cyanobacteria
A novel NDH-1L-CpcG2-phycobilisome-PSI supercomplex essential to cyclic electron transport was identified in Synechocystis sp. strain PCC 6803.
- 12 September 2016
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 172 (3) , 1451-1464
Open AccessThe NDH-1L-PSI Supercomplex Is Important for Efficient Cyclic Electron Transport in Cyanobacteria
A novel NDH-1L-CpcG2-phycobilisome-PSI supercomplex essential to cyclic electron transport was identified in Synechocystis sp. strain PCC 6803.
- Open Access
- 18 April 2016
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 171 (2) , 864-877
A Cytoplasmic Protein Ssl3829 Is Important for NDH-1 Hydrophilic Arm Assembly in Synechocystis sp. Strain PCC 6803
A 10-kD cytoplasmic protein, Ssl3829, plays an important role in NDH-1 assembly by accumulating subunit maturation factor and assembly intermediate in a cyanoba
- 18 April 2016
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 171 (2) , 864-877
Open AccessA Cytoplasmic Protein Ssl3829 Is Important for NDH-1 Hydrophilic Arm Assembly in Synechocystis sp. Strain PCC 6803
A 10-kD cytoplasmic protein, Ssl3829, plays an important role in NDH-1 assembly by accumulating subunit maturation factor and assembly intermediate in a cyanoba
- Open Access
- 14 April 2015
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 168 (2) , 443-451
Subunit Q Is Required to Stabilize the Large Complex of NADPH Dehydrogenase in Synechocystis sp. Strain PCC 6803
Two major complexes of NADPH dehydrogenase (NDH-1) have been identified in cyanobacteria. A large complex (NDH-1L) contains NdhD1, NdhF1, and NdhP, which are absent in a medium size complex (NDH-1M). They play important roles in respiration, NDH-1-dependent cyclic electron transport around photosystem I, and CO2 uptake. Two mutants sensitive to high light for growth and impaired in cyclic electron transport around photosystem I were isolated from the cyanobacterium Synechocystis sp. strain PCC 6803 transformed with a transposon-bearing library. Both mutants had a tag in an open reading frame encoding a product highly homologous to NdhQ, a single-transmembrane small subunit of the NDH-1L complex, identified in Thermosynechococcus elongatus by proteomics strategy. Deletion of ndhQ disassembled about one-half of the NDH-1L to NDH-1M and consequently impaired respiration, but not CO2 uptake. During prolonged incubation of the thylakoid membrane with n-dodecyl-β-d-maltoside at room temperature, the rest of the NDH-1L in ΔndhQ was disassembled completely to NDH-1M and was much faster than in the wild type. In the ndhP-deletion mutant (ΔndhP) background, absence of NdhQ almost completely disassembled the NDH-1L to NDH-1M, similar to the results observed in the ΔndhD1/ΔndhD2 mutant. We therefore conclude that both NdhQ and NdhP are essential to stabilize the NDH-1L complex.
- 14 April 2015
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 168 (2) , 443-451
Open AccessSubunit Q Is Required to Stabilize the Large Complex of NADPH Dehydrogenase in Synechocystis sp. Strain PCC 6803
Two major complexes of NADPH dehydrogenase (NDH-1) have been identified in cyanobacteria. A large complex (NDH-1L) contains NdhD1, NdhF1, and NdhP, which are absent in a medium size complex (NDH-1M). They play important roles in respiration, NDH-1-dependent cyclic electron transport around photosystem I, and CO2 uptake. Two mutants sensitive to high light for growth and impaired in cyclic electron transport around photosystem I were isolated from the cyanobacterium Synechocystis sp. strain PCC 6803 transformed with a transposon-bearing library. Both mutants had a tag in an open reading frame encoding a product highly homologous to NdhQ, a single-transmembrane small subunit of the NDH-1L complex, identified in Thermosynechococcus elongatus by proteomics strategy. Deletion of ndhQ disassembled about one-half of the NDH-1L to NDH-1M and consequently impaired respiration, but not CO2 uptake. During prolonged incubation of the thylakoid membrane with n-dodecyl-β-d-maltoside at room temperature, the rest of the NDH-1L in ΔndhQ was disassembled completely to NDH-1M and was much faster than in the wild type. In the ndhP-deletion mutant (ΔndhP) background, absence of NdhQ almost completely disassembled the NDH-1L to NDH-1M, similar to the results observed in the ΔndhD1/ΔndhD2 mutant. We therefore conclude that both NdhQ and NdhP are essential to stabilize the NDH-1L complex.
- 3 August 2011
- Published by Springer Nature
- p. 625-650
The Uptake of CO2 by Cyanobacteria and Microalgae
- 3 August 2011
- Published by Springer Nature
- p. 625-650
The Uptake of CO2 by Cyanobacteria and Microalgae
- 25 April 2011
- Published by Wiley in Environmental Microbiology
- Vol. 13 (7) , 1767-1777
Cross‐talk between photomixotrophic growth and CO 2 ‐concentrating mechanism in Synechocystis sp. strain PCC 6803
Summary: Simultaneous catabolic and anabolic glucose metabolism occurs in the same compartment during photomixotrophic growth of the model cyanobacterium Synechocystis sp. PCC 6803. The presence of glucose is stressful to the cells; it is reflected in the high frequency of suppression mutations in glucose‐sensitive mutants. We show that glucose affects many cellular processes. It stimulates respiration and the rate of photosynthesis and quantum yield in low‐ but not high‐CO 2 ‐grown cells. Fluorescence and thermoluminescence parameters of photosystem II are also affected but the results did not lend support to sustained glucose driven over reduction in the light. Glucose‐sensitive mutants such as Δ pmgA (impaired in photomixotrophic growth) and Δ hik31 (lacking histidine kinase 31) are far more susceptible under high than low air level of CO 2 . A glycine to tryptophan mutation in position 354 in NdhF3, involved in the high‐affinity CO 2 uptake, rescued Δ pmgA . A rise in the apparent photosynthetic affinity to external inorganic carbon is observed in high‐CO 2 ‐grown wild‐type cells after the addition of glucose, but not in mutant Δ pmgA . This is attributed to upregulation of certain low‐CO 2 ‐induced genes, involved in inorganic carbon uptake, in the wild type but not in Δ pmgA . These data uncovered a new level of interaction between CO 2 fixation (and the CO 2 ‐concentrating mechanism) and photomixotrophic growth in cyanobacteria.
- 25 April 2011
- Published by Wiley in Environmental Microbiology
- Vol. 13 (7) , 1767-1777
Cross‐talk between photomixotrophic growth and CO 2 ‐concentrating mechanism in Synechocystis sp. strain PCC 6803
Summary: Simultaneous catabolic and anabolic glucose metabolism occurs in the same compartment during photomixotrophic growth of the model cyanobacterium Synechocystis sp. PCC 6803. The presence of glucose is stressful to the cells; it is reflected in the high frequency of suppression mutations in glucose‐sensitive mutants. We show that glucose affects many cellular processes. It stimulates respiration and the rate of photosynthesis and quantum yield in low‐ but not high‐CO 2 ‐grown cells. Fluorescence and thermoluminescence parameters of photosystem II are also affected but the results did not lend support to sustained glucose driven over reduction in the light. Glucose‐sensitive mutants such as Δ pmgA (impaired in photomixotrophic growth) and Δ hik31 (lacking histidine kinase 31) are far more susceptible under high than low air level of CO 2 . A glycine to tryptophan mutation in position 354 in NdhF3, involved in the high‐affinity CO 2 uptake, rescued Δ pmgA . A rise in the apparent photosynthetic affinity to external inorganic carbon is observed in high‐CO 2 ‐grown wild‐type cells after the addition of glucose, but not in mutant Δ pmgA . This is attributed to upregulation of certain low‐CO 2 ‐induced genes, involved in inorganic carbon uptake, in the wild type but not in Δ pmgA . These data uncovered a new level of interaction between CO 2 fixation (and the CO 2 ‐concentrating mechanism) and photomixotrophic growth in cyanobacteria.
- Open Access
- 10 September 2008
- Published by Oxford University Press (OUP) in Plant and Cell Physiology
- Vol. 49 (11) , 1672-1677
Properties of Mutants of Synechocystis sp. Strain PCC 6803 Lacking Inorganic Carbon Sequestration Systems
A mutant (Δ5) of Synechocystis sp. strain PCC 6803 constructed by inactivating five inorganic carbon sequestration systems did not take up CO2 or HCO3− and was unable to grow in air with or without glucose. The Δ4 mutant in which BicA is the only active inorganic carbon sequestration system showed low activity of HCO3− uptake and grew under these conditions but more slowly than the wild-type strain. The Δ5 mutant required 1.7% CO2 to attain half the maximal growth rate. Electron transport activity of the mutants was strongly inhibited under high light intensities, with the Δ5 mutant more susceptible to high light than the Δ4 mutant. The results implicated the significance of carbon sequestration in dissipating excess light energy.
- 10 September 2008
- Published by Oxford University Press (OUP) in Plant and Cell Physiology
- Vol. 49 (11) , 1672-1677
Open AccessProperties of Mutants of Synechocystis sp. Strain PCC 6803 Lacking Inorganic Carbon Sequestration Systems
A mutant (Δ5) of Synechocystis sp. strain PCC 6803 constructed by inactivating five inorganic carbon sequestration systems did not take up CO2 or HCO3− and was unable to grow in air with or without glucose. The Δ4 mutant in which BicA is the only active inorganic carbon sequestration system showed low activity of HCO3− uptake and grew under these conditions but more slowly than the wild-type strain. The Δ5 mutant required 1.7% CO2 to attain half the maximal growth rate. Electron transport activity of the mutants was strongly inhibited under high light intensities, with the Δ5 mutant more susceptible to high light than the Δ4 mutant. The results implicated the significance of carbon sequestration in dissipating excess light energy.
- 6 February 2007
- Published by Springer Nature in Photosynthesis Research
- Vol. 93 (1-3) , 69-77
Cyanobacterial NADPH dehydrogenase complexes
Cyanobacteria possess functionally distinct multiple NADPH dehydrogenase (NDH-1) complexes that are essential to CO2 uptake, photosystem-1 cyclic electron transport and respiration. The unique nature of cyanobacterial NDH-1 complexes is the presence of subunits involved in CO2 uptake. Other than CO2 uptake, chloroplastic NDH-1 complex has a similar role as cyanobacterial NDH-1 complexes in photosystem-1 cyclic electron transport and respiration (chlororespiration). In this mini-review we focus on the structure and function of cyanobacterial NDH-1 complexes and their phylogeny. The function of chloroplastic NDH-1 complex and characteristics of plants defective in NDH-1 are also described for comparison.
- 6 February 2007
- Published by Springer Nature in Photosynthesis Research
- Vol. 93 (1-3) , 69-77
Cyanobacterial NADPH dehydrogenase complexes
Cyanobacteria possess functionally distinct multiple NADPH dehydrogenase (NDH-1) complexes that are essential to CO2 uptake, photosystem-1 cyclic electron transport and respiration. The unique nature of cyanobacterial NDH-1 complexes is the presence of subunits involved in CO2 uptake. Other than CO2 uptake, chloroplastic NDH-1 complex has a similar role as cyanobacterial NDH-1 complexes in photosystem-1 cyclic electron transport and respiration (chlororespiration). In this mini-review we focus on the structure and function of cyanobacterial NDH-1 complexes and their phylogeny. The function of chloroplastic NDH-1 complex and characteristics of plants defective in NDH-1 are also described for comparison.
- 1 August 2003
- Published by Springer Nature in Photosynthesis Research
- Vol. 77 (2-3) , 105-115
Inorganic carbon acquisition systems in cyanobacteria
This minireview focuses on the mechanism of inorganic carbon uptake in cyanobacteria and in particular the two CO2-uptake systems and two bicarbonate transporters recently identified in Synechocycstis...
- 1 August 2003
- Published by Springer Nature in Photosynthesis Research
- Vol. 77 (2-3) , 105-115
Inorganic carbon acquisition systems in cyanobacteria
This minireview focuses on the mechanism of inorganic carbon uptake in cyanobacteria and in particular the two CO2-uptake systems and two bicarbonate transporters recently identified in Synechocycstis...
- 1 January 1987
- Published by Springer Nature
- p. 297-300
A Model for Inorganic Carbon Accumulation in Cyanobacteria
- 1 January 1987
- Published by Springer Nature
- p. 297-300
A Model for Inorganic Carbon Accumulation in Cyanobacteria